Human methionine aminopeptidase type 2 in complex with L- and D-methionine

被引：8
|
作者：
Nonato, MC [1 ]
Widom, J [1 ]
Clardy, J [1 ]
机构：
[1] Cornell Univ, Baker Lab, Dept Chem & Biol Chem, Ithaca, NY 14853 USA
来源：
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2006年 / 16卷 / 10期
关键词：
methionine aminopeptidase; X-ray crystallography; enantiomer discrimination; pi-cation interaction; D-methionine; L-methionine;
D O I：
10.1016/j.bmcl.2006.02.047
中图分类号：
R914 [药物化学];
学科分类号：
100701 ;
摘要：
Human methionine aminopeptidase type 2 (hMetAP-2) was identified as the molecular target of anti-angiogenic agents such as fumagillin and its analogues. We describe here the crystal structure of hMetAP-2 in complex With L-methionine and D-methionine at 1.9 and 2.0 angstrom resolution, respectively. The comparison of the structure of the two complexes establishes the basis of enantiomer discrimination and provides some considerations for the design of selective MetAP-2 inhibitors. (C) 2006 Elsevier Ltd. All rights reserved.
引用
收藏
页码：2580 / 2583
页数：4
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